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- W1880245975 abstract "Perlucin isolated from abalone nacre consists of 155 amino acids including a glycosylated asparagine. The sequence of the first 130 amino acids shows a high similarity to the C-type carbohydrate-recognition domains of asialoglycoprotein receptors and other members of the group of C-type lectins but also a weaker similarity to related proteins without carbohydrate-binding activity. This C-type module is followed by a short C-terminal domain containing two almost identical sequence repeats with a length of 10 amino acids. Solid phase assays show a divalent metal ion-dependent binding of perlucin to (neo)glycoproteins containing d-galactose or d-mannose/d-glucose indicating that perlucin is a functional C-type lectin with broad carbohydrate-binding specificity. Our results also indicate that it may be difficult to predict carbohydrate-binding specificity and the occurrence of alternative binding configurations by amino-acid sequence comparisons and homology modeling." @default.
- W1880245975 created "2016-06-24" @default.
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- W1880245975 date "2000-08-01" @default.
- W1880245975 modified "2023-09-25" @default.
- W1880245975 title "The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin" @default.
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- W1880245975 doi "https://doi.org/10.1046/j.1432-1327.2000.01602.x" @default.
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